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Degree of sialylation and fucosylation of plasma and amniotic immunoglobulin G changes progressively during normal pregnancy.
MedLine Citation:
PMID:  22495687     Owner:  NLM     Status:  Publisher    
OBJECTIVE: Terminal-located glycotopes on immunoglobulin G (IgG) are potential ligands engaged in the interactions that may modulate the biological activities of IgG. The expressions of sialic acid and fucose residues on amniotic IgG were evaluated here in relation to the progression of normal human pregnancy. METHODS: Sialyl-glycotope and fucosyl-glycotope expressions on maternal plasma and amniotic IgG were determined by lectin-IgG-ELISA. RESULTS: The amniotic and maternal plasma IgG concentrations and a degree of α2,6-sialylation and α1,6-fucosylation of maternal plasma IgG were almost unaltered during the normal pregnancy. The plasma IgG of pregnant and nonpregnant women did not contain α2,3-linked sialic acid and α1,3-linked and α1,2-linked fucoses. In contrast, the amniotic IgG from the second trimester was decorated by α2,3-linked sialic acids, α2,6-linked sialic acids, and α1,6-linked fucose, whereas the α1,3-linked and α1,2-linked fucoses were weakly expressed. During 35-37 weeks of gestation, all the parameters increased significantly, and they remained almost at the same levels throughout 35-42 weeks, including the delivery. However, they were significantly higher in the postdate pregnancy group. CONCLUSION: The degree of sialylation and fucosylation of amniotic IgG was associated with the progression of normal pregnancy. © 2012 John Wiley & Sons, Ltd.
Magdalena Orczyk-Pawiłowicz; Daria Augustyniak; Lidia Hirnle; Iwona Kątnik-Prastowska
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-4-11
Journal Detail:
Title:  Prenatal diagnosis     Volume:  -     ISSN:  1097-0223     ISO Abbreviation:  -     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-4-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8106540     Medline TA:  Prenat Diagn     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 John Wiley & Sons, Ltd.
Department of Chemistry and Immunochemistry, Wrocław Medical University, Wrocław, Poland.
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